《Nature,4月24日,Neutralization of SARS-CoV-2 spike pseudotyped virus by recombinant ACE2-Ig》

  • 来源专题:COVID-19科研动态监测
  • 编译者: zhangmin
  • 发布时间:2020-04-25
  • Neutralization of SARS-CoV-2 spike pseudotyped virus by recombinant ACE2-Ig

    Changhai Lei, Kewen Qian, Tian Li, Sheng Zhang, Wenyan Fu, Min Ding & Shi Hu

    Nature Communications volume 11, Article number: 2070 (2020)


    Severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) emerged in Wuhan, China, at the end of 2019, and there are currently no specific antiviral treatments or vaccines available. SARS-CoV-2 has been shown to use the same cell entry receptor as SARS-CoV, angiotensin-converting enzyme 2 (ACE2). In this report, we generate a recombinant protein by connecting the extracellular domain of human ACE2 to the Fc region of the human immunoglobulin IgG1. A fusion protein containing an ACE2 mutant with low catalytic activity is also used in this study.

  • 《4月24日_第二军医大学等团队发现ACE2-Ig重组蛋白可中和SARS-CoV-2棘突蛋白假型病毒》

    • 来源专题:COVID-19科研动态监测
    • 编译者:xuwenwhlib
    • 发布时间:2020-04-25
    • 信息名称: 第二军医大学等团队发现ACE2-Ig重组蛋白可中和SARS-CoV-2棘突蛋白假型病毒 1.时间:2020年4月24日 2.机构或团队:海军军医大学(第二军医大学)、上海交通大学医学院和Pharchoice Therapeutics Inc 3.事件概要: 4月24日,Nature Communications发表了题为“Neutralization of SARS-CoV-2 spike pseudotyped virus by recombinant ACE2-Ig”的文章。 SARS-CoV-2于2019年底在中国武汉出现,目前尚无特异性抗病毒治疗方法或疫苗。SARS-CoV-2与SARS-CoV一样利用相同的细胞进入受体—血管紧张素转换酶2(ACE2)。在本文章中,研究团队通过将人ACE2的胞外区连接到人免疫球蛋白IgG1的Fc区来产生重组蛋白。本研究还使用了一个包含具有低催化活性ACE2突变体的融合蛋白。然后对融合蛋白进行表征。这两种融合蛋白均对SARS-CoV和SARS-CoV-2的受体结合域具有高度的结合亲和力,并在小鼠体内表现出良好的药理特性。此外,该融合蛋白在体外可中和SARS-CoV或SARS-CoV-2的棘突蛋白假型病毒。由于这些融合蛋白对冠状病毒具有交叉反应性,因此在SARS-CoV-2的诊断、预防和治疗中具有潜在的应用价值。 4.附件: 原文链接 https://www.nature.com/articles/s41467-020-16048-4
  • 《Nature,3月11日,SARS-CoV-2 neutralizing human recombinant antibodies selected from pre-pandemic healthy donors binding at RBD-ACE2 interface》

    • 来源专题:COVID-19科研动态监测
    • 编译者:zhangmin
    • 发布时间:2021-03-15
    • SARS-CoV-2 neutralizing human recombinant antibodies selected from pre-pandemic healthy donors binding at RBD-ACE2 interface Federico Bertoglio, Doris Meier, […]Michael Hust Nature Communications volume 12, Article number: 1577 (2021) Abstract COVID-19 is a severe acute respiratory disease caused by SARS-CoV-2, a new recently emerged sarbecovirus. This virus uses the human ACE2 enzyme as receptor for cell entry, recognizing it with the receptor binding domain (RBD) of the S1 subunit of the viral spike protein. We present the use of phage display to select anti-SARS-CoV-2 spike antibodies from the human naïve antibody gene libraries HAL9/10 and subsequent identification of 309 unique fully human antibodies against S1. 17 antibodies are binding to the RBD, showing inhibition of spike binding to cells expressing ACE2 as scFv-Fc and neutralize active SARS-CoV-2 virus infection of VeroE6 cells. The antibody STE73-2E9 is showing neutralization of active SARS-CoV-2 as IgG and is binding to the ACE2-RBD interface. Thus, universal libraries from healthy human donors offer the advantage that antibodies can be generated quickly and independent from the availability of material from recovering patients in a pandemic situation.